This proposal focuses on the relationship between glucocorticoid receptor (GR) function and dynamic transformations of GR by phosphorylation and association with heat shock proteins. Previous work by the principal investigator has identified in detail the sites at which GR is phosphorylated, and has shown cell-cycle dependent changes in GR phosphorylation and heat shock protein association/dissociation. The present proposal will extend these studies, addressing 1) the role of GR phosphorylation in GR function; 2) the role of cell-cycle dependent kinases in this phosphorylation; 3) the possibility that estrogen in progesterone receptors also traverse ATP-dependent cycles.